3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.35)
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase
     (EC 4.2.1.17)
     (EC 5.3.3.8)

Gene name

OrderedLocusNames:

RP560

From

Rickettsia prowazekii

[TaxID: 782]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Madrid E;
DOI=10.1038/24094; PubMed=9823893 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.;
"The genome sequence of Rickettsia prowazekii and the origin of mitochondria.";
Nature 396:133-140(1998).

Comments

CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.
CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O.
CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
SIMILARITY: In the N-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
SIMILARITY: In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ235272; CAA15008.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F71660; F71660.

RefSeq

NP_220931.1; -.

3D structure databases

HSSP

P00348; 3HDH. [HSSP ENTRY / PDB]

ModBase

Q9ZCZ1.

Enzyme and pathway databases

BioCyc

RPRO272947:RP560-MON; -.

Ontologies

GO:0003857;	Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from EC).
GO:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
GO:0004165;	Molecular function: dodecenoyl-CoA delta-isomerase activity (inferred from electronic annotation from EC).
GO:0004300;	Molecular function: enoyl-CoA hydratase activity (inferred from electronic annotation from EC).
GO:0006631;	Biological process: fatty acid metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006180; 3-OHacyl-CoA_DHase_CS.
IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF00725; 3HCDH; 1.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00067; 3HCDH; FALSE_NEG.
PS00166; ENOYL_COA_HYDRATASE; FALSE_NEG.

ProtoNet

Q9ZCZ1.

Genome annotation databases

GeneID

883251; -.

GenomeReviews

AJ235269_GR; RP560.

KEGG

rpr:RP560; -.

Phylogenomic databases

HOGENOM

Q9ZCZ1; -.

Genome annotation databases

CMR

Q9ZCZ1; RP560.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 720`	`720`	`Putative fatty acid oxidation complex trifunctional enzyme.`	`PRO_0000285698`
`REGION`	`1 384`	`384`	`3-hydroxyacyl-CoA dehydrogenase.`
`REGION`	`453 720`	`268`	`Enoyl-CoA hydratase/isomerase.`

Sequence information

Length: 720 AA [This is the length of the unprocessed precursor]

Molecular weight: 81403 Da [This is the MW of the unprocessed precursor]

CRC64: BAEC37A40044234E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQNEIKKVCV IGAGVMGSGI AALIANSSHQ VVLLDILDKD SNDPNKIVKN SVKNLHKQKL 

        70         80         90        100        110        120 
SPLSFPDKVN FITIGNLEHD LDLIKECNLV IEVIVEKLEI KHQLYNKIIP YLKEDAIIAS 

       130        140        150        160        170        180 
NTSTLPLKKL KVNLPNNIKS RFVITHFFNP PRYMELVELI IDHTIKDEVI EKVSVFLTKM 

       190        200        210        220        230        240 
LGKTIIKCND TPGFIANRVG CFLLELVVHK AIAQNLNFVT IDQIFSRCLG LPNTGIFGLY 

       250        260        270        280        290        300 
DLIGHDVMKL ISSSLISALP KSDDYHRIYT NTKVFDKMIE HNLIGRKGEG GFYRLSVSNG 

       310        320        330        340        350        360 
KKIKEVINIS DLSYHPVQKV DISFNSLNEL LSSNSIYGKF FSEIITEFYI YLTSLVPSVT 

       370        380        390        400        410        420 
NNIYDIDTTM KLGYSWHYGP FELLTIAVKN GWNLIIKNAD LMNIPLPKYL ASKEYQKIDK 

       430        440        450        460        470        480 
QKFNSKKDFL QESKIVLSND SANLIHYCEN LVFVITTKMN SLNHNVFYLL QEAVSKAENY 

       490        500        510        520        530        540 
GKNLYIYPQG NNFSAGADLK LILSYIQDGN FHNLENLLKL GQQTMRYLKY SSVHIISCAR 

       550        560        570        580        590        600 
GVALGGGCEL LLNSSYIVAN QELNAGLIEL GVGLIPGWTG VTEMFARSNG NKTKLIRNIK 

       610        620        630        640        650        660 
NIIEQNKTSS ADYFKADYGI KNMQVNMNKH YILDDALKLR ISKKIVSIPN KITLPKINIV 

       670        680        690        700        710        720 
SEIDTSKYNE LQNKVLNKFQ NIIDKHNEIS EAELLTYERE MFLELAKTPQ TIEKLQAIVG

Q9ZCZ1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools